scholarly journals Tim50 inTrypanosoma bruceiPossesses a Dual Specificity Phosphatase Activity and Is Critical for Mitochondrial Protein Import

2012 ◽  
Vol 288 (5) ◽  
pp. 3184-3197 ◽  
Author(s):  
Melanie R. Duncan ◽  
Marjorie Fullerton ◽  
Minu Chaudhuri
Author(s):  
George T. Lountos ◽  
Scott Cherry ◽  
Joseph E. Tropea ◽  
David S. Waugh

4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.


Cell ◽  
2000 ◽  
Vol 100 (5) ◽  
pp. 551-560 ◽  
Author(s):  
Yoshito Abe ◽  
Toshihiro Shodai ◽  
Takanori Muto ◽  
Katsuyoshi Mihara ◽  
Hisayoshi Torii ◽  
...  

2021 ◽  
Author(s):  
Liam P. Coyne ◽  
Xiaowen Wang ◽  
Jiyao Song ◽  
Ebbing de Jong ◽  
Karin Schneider ◽  
...  

2016 ◽  
Vol 397 (11) ◽  
pp. 1097-1114 ◽  
Author(s):  
Sebastian P. Straub ◽  
Sebastian B. Stiller ◽  
Nils Wiedemann ◽  
Nikolaus Pfanner

Abstract Mitochondria contain elaborate machineries for the import of precursor proteins from the cytosol. The translocase of the outer mitochondrial membrane (TOM) performs the initial import of precursor proteins and transfers the precursors to downstream translocases, including the presequence translocase and the carrier translocase of the inner membrane, the mitochondrial import and assembly machinery of the intermembrane space, and the sorting and assembly machinery of the outer membrane. Although the protein translocases can function as separate entities in vitro, recent studies revealed a close and dynamic cooperation of the protein import machineries to facilitate efficient transfer of precursor proteins in vivo. In addition, protein translocases were found to transiently interact with distinct machineries that function in the respiratory chain or in the maintenance of mitochondrial membrane architecture. Mitochondrial protein import is embedded in a regulatory network that ensures protein biogenesis, membrane dynamics, bioenergetic activity and quality control.


2007 ◽  
Vol 17 (9) ◽  
pp. 456-464 ◽  
Author(s):  
Michael J. Baker ◽  
Ann E. Frazier ◽  
Jacqueline M. Gulbis ◽  
Michael T. Ryan

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